Predicted secondary structure for the Src homology 3 domain

J Mol Biol. 1993 Jan 20;229(2):295-305. doi: 10.1006/jmbi.1993.1035.

Abstract

A de novo secondary structure prediction has been prepared for Src homology domain 3, in advance of any crystallographic information concerning any member of this interesting protein family. The prediction can be compared with a crystal structure that will be published in Nature on October 29, 1992. The prediction is based on analysis of a multiple alignment of homologous proteins. The patterns of variation and conservation of amino acids across the alignment allow the determination of surface and internal positions, which then allow the assignment of secondary structure. The prediction is quite different both in method and, in this case, result from predictions based on propensities (e.g. Garnier-Osgurthorpe-Robson) of particular amino acids to appear in particular types of secondary structure.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chickens
  • Crystallography
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Phylogeny
  • Protein Structure, Secondary*
  • Proto-Oncogene Proteins pp60(c-src) / chemistry*
  • Proto-Oncogene Proteins pp60(c-src) / classification
  • Sequence Homology, Amino Acid

Substances

  • Peptide Fragments
  • Proto-Oncogene Proteins pp60(c-src)